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insulin

✓ Approved

MJ Biotech · INSR · 重组蛋白

什么是 insulin？

insulin 是一种重组蛋白，由MJ Biotech研发。该药已获批，用于治疗相关适应症，给药途径：Injectable (Others)。

药物档案

公司MJ Biotech
药物类别重组蛋白
分子靶点INSR
给药途径Injectable (Others)
状态Approved
来源： ClinicalTrials.gov, MJ Biotech

作用机制

分子靶点

insulin 作用于 1 个分子靶点：

INSRinsulin receptor (CD220, HHF5)
需要更深入的分析？Noah AI 可解释复杂机制并与同类药物比较。

治疗适应症

insulin 针对 1 个适应症，涉及 1 个治疗领域。

治疗领域疾病/病症分期
InvestigationsGlucose tolerance test abnormal✓ Approved

相关研究文献

PubMedBiotechnology journal2026-10-27

Effectively Heterologous Synthesis of Lovastatin in Aspergillus niger by Improved Supply of Precursor Monacolin J.

Lu Feifei F, Liu Qi Q, Qiu Yanqing Y, Zeng Xu X et al.

Using transformation-associated recombination (TAR) technology, a lovastatin biosynthetic gene cluster was assembled in Saccharomyces cerevisiae BY4741, in which pathway-related enzyme genes were controlled by strong fungal promoters and terminators. Using Aspergillus niger SH-2 as the starting strain, a copy of Monacolin J (MJ) and a copy of lovastatin expression cassette were integrated into its genome, MJ heterologous expression strains and lovastatin heterologous expression strains were successively constructed. To facilitate the synthesis of MJ and lovastatin, ATP-dependent citrate lyase (ACL) and acetyl-CoA carboxylase (ACC) were overexpressed in the MJ- and lovastatin-engineered strains. For fermentation optimization, various carbon sources were tested to determine the best one. Furthermore, the roles of glutamic acid, methionine, and linoleic acid in the production of MJ and lovastatin were investigated. Finally, in a 500 mL shake flask with 100 mL of liquid medium, using hydrolyzed starch as the carbon source and adding 10 mM glutamate, a MJ titer of 1606 mg/L and a lovastatin of 1345 mg/L were obtained, and after overexpressing ACL and ACC enzymes in the MJ strain, a MJ titer of 1786 mg/L were obtained. During fed-batch fermentation in a 2-L bioreactor, the lovastatin yield reached 2915 mg/L.

PMID 42937016
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PubMedInternational journal of molecular sciences2026-10-27

Toxins and Antivenoms of Latrodectus tredecimguttatus: Molecular Mechanisms, Antibody Development, and Evidence from Other Latrodectus Species.

Rakhim Marziya M, Abekova Assima A, Shynykul Zhanserik Z, Koilybayeva Moldir M et al.

Latrodectus tredecimguttatus envenomation causes latrodectism, a neurotoxic syndrome driven primarily by α-latrotoxin (α-LTX)-mediated dysregulation of neurotransmitter release. This review examines the development and therapeutic application of specific immunoglobulins against L. tredecimguttatus toxins, integrating toxin diversity, α-LTX mechanisms, antibody production, preclinical neutralization, and clinical use. Eggs and spiderlings also contain bioactive proteins, including Latroeggtoxin-I and Latroeggtoxin-IV, although their relevance to human envenomation and antivenom development remains uncertain. α-LTX acts through receptor engagement, membrane pore formation, Ca2+ influx, and receptor-mediated signaling, providing potential targets for antibody neutralization. Conventional antivenoms rely mainly on animal-derived polyclonal immunoglobulins, whereas phage display and recombinant engineering enable fully human monoclonal antibodies with defined specificity and high affinity. Preclinical studies demonstrate neutralization across cellular, electrophysiological, ex vivo, and in vivo models, but methodological heterogeneity and variable cross-species activity complicate efficacy comparisons. Recombinant human antibodies offer improved molecular definition, reproducibility, and engineering potential, although clinical efficacy remains unestablished. Future development should prioritize standardized neutralization assays, clinically relevant post-exposure models, systematic cross-neutralization studies, and recombinant antibody combinations to achieve broader toxin coverage and safer, more standardized, reproducible, and clinically applicable immunotherapy for L. tredecimguttatus envenomation.

PMID 42941881
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PubMedCurrent issues in molecular biology2026-10-27

Molecular Characterization of Recombinant Human Inhibin α- and βB-Subunits and Activin A (βA-βA) Using Raman Spectroscopy.

Xiao Weiyu W, Dai Yuzhen Y, Quijano Sofia Martinez Gallardo SMG, Kotsifaki Domna G DG et al.

Members of the transforming growth factor-β (TGF-β) superfamily, including inhibins and activins, are structurally related signaling proteins that regulate reproductive and endocrine physiology. Although these proteins share a conserved cystine-knot architecture, differences in subunit composition and molecular organization contribute to distinct biological activities and can complicate their analytical discrimination. Here, Raman spectroscopy was used to characterize recombinant human inhibin α-subunit (INHA), recombinant human inhibin βB-subunit (INHBB (βB-subunit)), and activin A (βA-βA homodimer) under identical experimental conditions using 532 nm excitation. Raman spectra were baseline-corrected, Savitzky-Golay-smoothed, and area-normalized. Distinct spectral features were observed across the 500-1800 cm-1 protein fingerprint region, particularly in the S-S stretching, aromatic amino acid residue, amide III, and amide I regions. The S-S stretching region showed the highest relative contribution in INHA, whereas differences in phenylalanine- and amide-associated bands further distinguished the three proteins. These findings show that Raman spectra may contain molecular information that can distinguish closely related inhibin/activin proteins under the investigated solid-state conditions. Raman spectroscopy therefore provides a label-free, complementary approach to the molecular fingerprinting of TGF-β superfamily proteins and may facilitate their molecular characterization.

PMID 42939518
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PubMedBiomedicines2026-10-27

Impaired Regulated Exocytosis and GLUT4 Trafficking in Dysferlin-Deficient Human Myoblasts: A Pilot Study.

Guerra-Fernández María José MJ, Vásquez Walter W, Almarza-Salazar Hugo H, Bertea-Seissus Constanza C et al.

Background/Objectives: Dysferlinopathies are inherited muscular dystrophies caused by DYSF mutations that lead to progressive muscle degeneration. Proteomic analyses of patient muscle reveal altered abundance of proteins involved in regulated exocytosis and energy metabolism, reflecting complex molecular remodeling within these pathways. However, whether dysferlin deficiency impairs GLUT4 exocytosis remains unknown. Methods: Immortalized human myoblasts from a healthy control (C25) and a dysferlinopathy patient (DYSF2) were used. Cytosolic Ca2+ was measured using Fura-2 and Fluo-4; submembrane Ca2+ dynamics were recorded with membrane-targeted sensor pN1-Lck-GCaMP3. Single exocytosis events induced by 10 µM ionomycin or 100 nM insulin were tracked with IRAP-pHluorin and total internal reflection fluorescence microscopy (TIRFM). GLUT4 puncta near the plasma membrane were quantified using immunofluorescence and visualized by TIRFM. Dysferlin-3HA was expressed to test rescue. Results: Both cell lines showed comparable cytosolic and submembrane Ca2+ responses to ionomycin. However, the frequency of IRAP-pHluorin exocytosis events evoked by both ionomycin and insulin was significantly reduced in DYSF2 myoblasts. Expression of dysferlin-3HA restored insulin-induced exocytosis in DYSF2 cells to control levels but failed to fully rescue ionomycin-induced events. Insulin increased the trafficking of GLUT4 puncta near the plasma membrane in C25 cells, whereas DYSF2 cells lacked this insulin-stimulated response. Conclusions: In the patient-derived cell line examined here, dysferlin deficiency impaired stimulus-evoked exocytosis and insulin-induced GLUT4 translocation without altering Ca2+ dynamics. The inability of dysferlin-3HA to significantly rescue ionomycin-induced exocytosis points to additional downstream defects, likely secondary proteomic alterations, that constrain full functional recovery.

PMID 42940013
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PubMedPharmaceuticals (Basel, Switzerland)2026-10-27

Natural Modulators of the PPARγ-Adiponectin Axis in Insulin Resistance: Structural Pharmacology, Receptor-State Selectivity, and Translational Readiness.

Floriana Vasilica Pirscoveanu Denisa PD, Trasca Diana-Maria DM, Kamal Adina Maria AM, Varut Renata Maria RM et al.

Insulin resistance reflects maladaptive communication among adipose tissue, the liver, skeletal muscle, immune cells, and the vasculature. Peroxisome proliferator-activated receptor gamma (PPARγ) is a validated insulin-sensitizing target, but classical full agonism couples metabolic efficacy to weight gain, fluid retention, and skeletal liability. This critical narrative review evaluates plant-derived and dietary molecules through a receptor-state framework that distinguishes direct binding from reporter activation and separates full agonism, partial agonism, selective modulation, antagonism with retained metabolic function, and post-translational control of PPARγ. Adiponectin is considered a functional inter-organ circuit linking adipocyte PPARγ activity to AdipoR1/AdipoR2 signaling, AMPK, PPARα, ceramide metabolism, glucose disposal, and fatty-acid oxidation. Amorfrutins provide the most coherent target-led natural-product evidence, whereas chelerythrine offers a structurally defined selective-modulation benchmark; honokiol, diosmin, betulinic acid, valerenic acid, punicic acid, alkamides, and defined extracts show heterogeneous mechanistic and translational maturity. Human evidence linking natural PPARγ ligands to verified target engagement and improved insulin sensitivity remains limited. We therefore propose a seven-stage translational roadmap connecting chemical identity, orthogonal binding, receptor-state pharmacology, cellular function, tissue exposure, mechanism-matched safety, and randomized human proof.

PMID 42943204
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PubMedMaterials (Basel, Switzerland)2026-10-27

Effect of the MOPA Laser Cleaning Parameters on the Surface Evolution of the Epoxy Coating on AH36 Steel.

Xing Fayu F, Du Xu X, Xu Fachen F, Li Haoxiang H et al.

High-power laser cleaning has been extensively adopted to remove organic coatings, but pulse duration, pulse energy, and overlap rate must be adjusted to limit residue and thermally affected surface modification. In this work, a 1000 W MOPA pulsed fiber laser was used to strip a 75 ± 5 μm thick iron-red epoxy primer from AH36 marine steel. Single-factor tests and an L9(33) orthogonal design were evaluated using image-derived paint removal rate (PRR), surface roughness (Ra), SEM morphology, and energy-dispersive X-ray spectroscopy (EDS); every processing condition was repeated on five independently prepared coupons. Increasing pulse energy from 5.0 to 12.5 mJ raised the mean PRR from 79.01% to 99.67%, although the improvement above 7.5 mJ was marginal. At 70% overlap, PRR reached 99.12%, Fe was 77.7 wt.%, C was 8.1 wt.%, and Ra reached 4.196 μm, showing that high Fe exposure alone did not define the best surface state. Descriptive range values from the replicated L9 runs gave the apparent PRR order overlap rate > power > pulse duration; since the archived worksheet retained only run means, the small differences among the ranges cannot be tested against within-run error and are not treated as statistically significant. Run 2 (300 ns, 6.00 mJ at 100 kHz, and 60% overlap) was selected from the tested combinations as a multi-index engineering compromise rather than as a predicted optimum. It produced PRR = 99.90% and Ra = 1.308 μm. Pull-off testing used three dollies per recoated condition; the mean strength of the laser-cleaned condition was 5.20 MPa and failure was predominantly cohesive within the epoxy.

PMID 42941078
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